1. Field of the Invention
The present invention relates to a grooved gel, and more specifically to a grooved gel arrangement wherein distortions and spreading (diffusion) of proteins within the gel are eliminated or at least minimized.
2. Description of Prior Art
The human body contains proteins which are remarkably diverse in size, architecture and biological responsibility. They range in molecular weight from a few thousand to more than a million. They may be stretched into long, strong fibers or coiled into compact globules. They exist in a variety of different forms, such as: structural proteins, connective-tissue proteins, contractile muscle proteins, enzymes, hormones, antibodies, transport molecules (such as the hemoglobin which carries oxygen to the cells), storage proteins, cell-surface receptors, and the like.
One of the traditional methods for separating proteins for the purpose of identification is electrophoresis, which simply means "carried by electricity". Proteins from, for example, a blood or urine sample, appropriately prepared, can be separated in an electrical field because each different type of protein is carried along at a slightly different speed, depending on the net electrical charge of a given molecule. This method, one-dimensional electrophoresis, has proven to be an extremely powerful scientific tool.
In the mid 1970s, two-dimensional techniques for separating proteins were developed. One such technique was designated "gel electrophoresis", and comprises a technique which differentiates proteins moving through a gel into clearly delineated bands which can be identified as specific proteins or groups of proteins. The method separates proteins moving in one direction by their electrical charge into single rows. Then, the gel is turned on its side, and a detergent is added to interact electrically with the proteins, causing them to move in a second direction, by which movement in the second direction they are sorted out by size. Moreover, when the two-dimensional gel is stained with a dye, the result is a grid-like series of protein "spots", the columns being separated horizontally by their electrical charge, and vertically by size. Such a "protein map" can separate a great many more proteins from a sample than is possible with one-dimensional electrophoresis.
Gels utilized in the latter manner can then be scanned, the gel being divided into a very large number (for example, one or two million) tiny squares, each square being examined and analyzed by well-known computer information processing techniques. Once each square is analyzed in detail, the corresponding data can be stored for future recall, enhancement, and display. Moreover, the density data can be converted into color differences for easier discrimination and viewing on a computerized display. In addition, the "background noise", typically present in such scan-derived information, can be filtered out by a computer system, and distortions in the gel itself can also be corrected. A detailed treatment of such two-dimensional electrophoretic procedures is set forth in "High Resolution Two-Dimensional Electrophoresis of Proteins", by Patrick H. O'Farrell, The Journal of Biological Chemistry, Volume 250, No. 10 (May 25, 1975), pages 4007-4021.
It should be recognized that, for the purpose of gel analysis using computerized scanning, it is important that resolution be minimized to the greatest extent possible. On the other hand, attempts to minimize resolution, have in the past, been thwarted by the occurrence of the phenomenon known as diffusion (spreading). That is, during the first-dimensional phase of the electrophoretic procedure, the proteins are distributed latitudinally across the gel, and then, during the second-dimensional phase of the procedure, the proteins are distributed longitudinally through the gel along respective paths or channels. During the latter procedure, diffusion (spreading) of the proteins can take place, thus providing a distorted distribution of the proteins, and this adversely affects the resolution which can be achieved by the gel scanning procedure.
In addition, during the fabrication of gels, the physical gel itself often becomes distorted, and this adversely affects the process by means of which the proteins are distributed latitudinally and longitudinally within the gel during the electrophoretic procedure. This amounts to a further cause of adverse diffusion (spreading) of the protein within the gel, thus further adversely affecting the data derived from scanning of the gel during the computer scanning phase of operation.